F172A_MOUSE
ID F172A_MOUSE Reviewed; 417 AA.
AC Q3TNH5; Q3TLW0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Cotranscriptional regulator FAM172A {ECO:0000305};
DE Flags: Precursor;
GN Name=Fam172a {ECO:0000312|MGI:MGI:1915925};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, FUNCTION, MUTAGENESIS OF
RP GLU-229; SER-294 AND 307-ARG--LEU-417, INTERACTION WITH AGO2, DISRUPTION
RP PHENOTYPE, AND IDENTIFICATION IN A COMPLEX WITH FAM172A; AGO2 AND CHD7.
RX PubMed=29311329; DOI=10.1073/pnas.1715378115;
RA Belanger C., Berube-Simard F.A., Leduc E., Bernas G., Campeau P.M.,
RA Lalani S.R., Martin D.M., Bielas S., Moccia A., Srivastava A.,
RA Silversides D.W., Pilon N.;
RT "Dysregulation of cotranscriptional alternative splicing underlies CHARGE
RT syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E620-E629(2018).
CC -!- FUNCTION: Plays a role in the regulation of alternative splicing, by
CC interacting with AGO2 and CHD7. Seems to be required for stabilizing
CC protein-protein interactions at the chromatin-spliceosome interface
CC (PubMed:29311329). May have hydrolase activity (PubMed:29311329).
CC {ECO:0000269|PubMed:29311329}.
CC -!- SUBUNIT: Interacts with AGO2 (PubMed:29311329). Found in a complex,
CC composed of AGO2, CHD7 and FAM172A (PubMed:29311329).
CC {ECO:0000269|PubMed:29311329}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29311329}. Cytoplasm
CC {ECO:0000269|PubMed:29311329}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:29311329}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3TNH5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TNH5-2; Sequence=VSP_031750;
CC Name=3;
CC IsoId=Q3TNH5-3; Sequence=VSP_031751, VSP_031752;
CC -!- DEVELOPMENTAL STAGE: Widely expressed during development.
CC {ECO:0000269|PubMed:29311329}.
CC -!- DISRUPTION PHENOTYPE: Homozygotes deficient mice die before postnatal
CC day 25. Mice display retinal coloboma, cleft palate, and hypoplastic
CC semicircular canals, retarded growth, genital anomalies and
CC malformation of the heart and cranial nerves. Mice display a complex
CC phenotype mimicking both the major and minor features of CHARGE
CC syndrome (CHARGES). {ECO:0000269|PubMed:29311329}.
CC -!- SIMILARITY: Belongs to the FAM172 family. {ECO:0000305}.
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DR EMBL; AK165273; BAE38114.1; -; mRNA.
DR EMBL; AK166285; BAE38682.1; -; mRNA.
DR EMBL; AC167171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT025642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49317.1; -. [Q3TNH5-1]
DR CCDS; CCDS49319.1; -. [Q3TNH5-3]
DR RefSeq; NP_001156892.1; NM_001163420.1. [Q3TNH5-3]
DR RefSeq; NP_612185.1; NM_138312.1. [Q3TNH5-1]
DR AlphaFoldDB; Q3TNH5; -.
DR SMR; Q3TNH5; -.
DR STRING; 10090.ENSMUSP00000133140; -.
DR ESTHER; mouse-f172a; Arb2_FAM172A.
DR GlyGen; Q3TNH5; 1 site.
DR iPTMnet; Q3TNH5; -.
DR PhosphoSitePlus; Q3TNH5; -.
DR EPD; Q3TNH5; -.
DR MaxQB; Q3TNH5; -.
DR PaxDb; Q3TNH5; -.
DR PeptideAtlas; Q3TNH5; -.
DR PRIDE; Q3TNH5; -.
DR ProteomicsDB; 267682; -. [Q3TNH5-1]
DR ProteomicsDB; 267683; -. [Q3TNH5-2]
DR ProteomicsDB; 267684; -. [Q3TNH5-3]
DR Antibodypedia; 2355; 50 antibodies from 15 providers.
DR Ensembl; ENSMUST00000099358; ENSMUSP00000096960; ENSMUSG00000064138. [Q3TNH5-3]
DR Ensembl; ENSMUST00000163257; ENSMUSP00000133140; ENSMUSG00000064138. [Q3TNH5-1]
DR GeneID; 68675; -.
DR KEGG; mmu:68675; -.
DR UCSC; uc007rgy.2; mouse. [Q3TNH5-1]
DR UCSC; uc007rha.2; mouse. [Q3TNH5-3]
DR CTD; 83989; -.
DR MGI; MGI:1915925; Fam172a.
DR VEuPathDB; HostDB:ENSMUSG00000064138; -.
DR eggNOG; KOG3967; Eukaryota.
DR GeneTree; ENSGT00530000063907; -.
DR HOGENOM; CLU_048484_2_0_1; -.
DR InParanoid; Q3TNH5; -.
DR OrthoDB; 1036194at2759; -.
DR PhylomeDB; Q3TNH5; -.
DR TreeFam; TF315960; -.
DR BioGRID-ORCS; 68675; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Fam172a; mouse.
DR PRO; PR:Q3TNH5; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3TNH5; protein.
DR Bgee; ENSMUSG00000064138; Expressed in spermatocyte and 221 other tissues.
DR ExpressionAtlas; Q3TNH5; baseline and differential.
DR Genevisible; Q3TNH5; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0014032; P:neural crest cell development; IMP:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR039929; FAM172A.
DR PANTHER; PTHR21357:SF3; PTHR21357:SF3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disease variant; Endoplasmic reticulum;
KW Glycoprotein; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..417
FT /note="Cotranscriptional regulator FAM172A"
FT /id="PRO_0000320932"
FT REGION 208..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 414..417
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 294
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:29311329"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..138
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031750"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031751"
FT VAR_SEQ 126..189
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031752"
FT MUTAGEN 229
FT /note="E->Q: Fails to interacts with AGO2. Decreases
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:29311329"
FT MUTAGEN 294
FT /note="S->A: Loss of nucleophilicity of Ser-294."
FT /evidence="ECO:0000269|PubMed:29311329"
FT MUTAGEN 307..417
FT /note="Missing: Fails to interact with AGO2."
FT /evidence="ECO:0000269|PubMed:29311329"
SQ SEQUENCE 417 AA; 48072 MW; 8FBE7D0873DA8109 CRC64;
MSISLSSLIF LPIWINMAQM QQGGSNETEQ TAALKDLLSR IDLDELMKKD EPPFDFPDTL
EGFEYAFNEK GQLRHIKTGE PFVFNYREDL HRWNQKRYEA LGEIITRYVY ELLESDCNLK
KISIPVDATE SEPKSFIFMS EDALTNPQKL MVLIHGSGVV RAGQWARRLI INEDLDSGTQ
IPFIKRAMDE GYGVIVLNPN ENYIEVEKQK MHKQSSSSDG TDEPAGKRER RDKVSKETKK
RRDFYEKYRN PQKEKEMMQL FIRENGSPEE HAVYVWDHFI AQAAAENVFF VAHSYGGLAF
VELMIQREAD VKSKVTAVAL TDSVHNVWHQ EAGKTIREWM RENCCNWVSS SEPLDTSVES
MLPDCPRVSA GTDRHELTSW KSFPSIFKFF AEASEAKSSS QKPALTRRSH RIKHEEL
